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CAZyme Information: MGYG000002225_01161

You are here: Home > Sequence: MGYG000002225_01161

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species CAG-873 sp900554265
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-873; CAG-873 sp900554265
CAZyme ID MGYG000002225_01161
CAZy Family GH32
CAZyme Description Levanase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
574 MGYG000002225_175|CGC1 63214.7 4.6467
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002225 2013827 MAG United States North America
Gene Location Start: 3020;  End: 4744  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.26 3.2.1.64 3.2.1.80 3.2.1.65 3.2.1.153

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH32 105 408 2.7e-85 0.9863481228668942

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd18622 GH32_Inu-like 4.16e-142 111 399 2 289
glycoside hydrolase family 32 protein such as Aspergillus ficuum endo-inulinase (Inu2). This subfamily of glycosyl hydrolase family GH32 includes endo-inulinase (inu2, EC 3.2.1.7), exo-inulinase (Inu1, EC 3.2.1.80), invertase (EC 3.2.1.26), and levan fructotransferase (LftA, EC 4.2.2.16), among others. These enzymes cleave sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose, thus named invertase (EC 3.2.1.26). These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. These enzymes are predicted to display a 5-fold beta-propeller fold as found for GH43 and CH68. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
COG1621 SacC 6.14e-123 93 568 21 481
Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism].
smart00640 Glyco_32 9.03e-123 105 536 1 437
Glycosyl hydrolases family 32.
pfam00251 Glyco_hydro_32N 2.21e-99 105 408 1 305
Glycosyl hydrolases family 32 N-terminal domain. This domain corresponds to the N-terminal domain of glycosyl hydrolase family 32 which forms a five bladed beta propeller structure.
TIGR01322 scrB_fam 3.72e-70 93 547 6 445
sucrose-6-phosphate hydrolase. [Energy metabolism, Biosynthesis and degradation of polysaccharides]

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QCD36721.1 2.98e-301 1 572 41 612
QCD40830.1 3.66e-299 1 572 31 598
QCP73719.1 3.66e-299 1 572 31 598
QCD43708.1 1.29e-293 1 572 24 595
ASB38314.1 5.49e-281 1 572 40 611

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1Y4W_A 6.71e-99 98 572 5 513
Crystalstructure of exo-inulinase from Aspergillus awamori in spacegroup P21 [Aspergillus awamori],1Y9G_A Crystal structure of exo-inulinase from Aspergillus awamori complexed with fructose [Aspergillus awamori],1Y9M_A Crystal structure of exo-inulinase from Aspergillus awamori in spacegroup P212121 [Aspergillus awamori]
3RWK_X 8.33e-83 95 574 23 515
Firstcrystal structure of an endo-inulinase, from Aspergillus ficuum: structural analysis and comparison with other GH32 enzymes. [Aspergillus ficuum],3SC7_X First crystal structure of an endo-inulinase, from Aspergillus ficuum: structural analysis and comparison with other GH32 enzymes. [Aspergillus ficuum]
3KF5_A 6.25e-75 87 548 1 482
ChainA, Invertase [Schwanniomyces occidentalis],3KF5_B Chain B, Invertase [Schwanniomyces occidentalis]
3KF3_A 8.12e-75 98 548 7 479
ChainA, Invertase [Schwanniomyces occidentalis],3KF3_B Chain B, Invertase [Schwanniomyces occidentalis]
3U75_A 5.90e-74 86 548 19 505
ChainA, Fructofuranosidase [Schwanniomyces occidentalis],3U75_B Chain B, Fructofuranosidase [Schwanniomyces occidentalis],3U75_C Chain C, Fructofuranosidase [Schwanniomyces occidentalis],3U75_D Chain D, Fructofuranosidase [Schwanniomyces occidentalis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P05656 9.29e-117 98 570 32 507
Levanase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacC PE=1 SV=1
Q96TU3 6.27e-98 98 572 24 532
Extracellular exo-inulinase inuE OS=Aspergillus awamori OX=105351 GN=inuE PE=1 SV=1
Q76HP6 8.83e-98 98 572 24 532
Extracellular exo-inulinase inuE OS=Aspergillus niger OX=5061 GN=inuE PE=1 SV=1
E1ABX2 8.83e-98 98 572 24 532
Extracellular exo-inulinase inuE OS=Aspergillus ficuum OX=5058 GN=exoI PE=1 SV=1
A2R0E0 9.64e-97 98 572 24 532
Extracellular exo-inulinase inuE OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=inuE PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000035 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002225_01161.